Epilepsy in Irish psychiatric inpatient settings

Aims To ascertain epilepsy prevalence in Irish psychiatric inpatient units and compliance with care planning guidelines. Methods Case records were reviewed in seven psychiatric inpatient units. Results The prevalence of epilepsy across seven psychiatric inpatient units (n=9/267) was three times that of general population estimates. Minimal data was recorded pertaining to seizure type (n=1,11.1%), triggers (n=2,22.2%), clinical investigations relating to epilepsy (n=2,22%) and no epilepsy risk assessments were recorded (n=0,0%). Conclusions The introduction of appropriate care plans is needed to optimise physical and mental wellbeing of those with epilepsy in psychiatric units.

NMR and computational evidence that high-affinity bradykinin receptor antagonists adopt C-terminal beta-turns.

Three tetrapeptides were prepared, each corresponding to the four C-terminal amino acid residues of highly potent, second-generation bradykinin receptor antagonists. The tetrapeptides are (IA) Ser-D-Phe-Oic-Arg, (IIA) Ser-D-Tic-Oic-Arg, and (IIIA) Ser-D-Hype(trans-propyl)-Oic-Arg. Solution conformations for each were determined by incorporating interproton distance restraints, determined by 2D NMR experiments performed in water at neutral pH, into a series of distance geometry/simulated annealing model building calculations. Similarly, systematic conformational analyses were performed for each using molecular mechanics calculations. Both the NMR-derived structures, as well as the calculated structures, are shown to adopt a beta-turn as the primary conformation. Excellent agreement between the predicted structures and the NMR-derived structures is demonstrated. Aside from being the first examples of linear tetrapeptides reported to be ordered in aqueous solvent, the results presented support the hypothesis that high-affinity bradykinin receptor antagonists must adopt C-terminal beta-turn conformations.

A novel beta-turn mimic useful for mapping the unknown topology of peptide receptors.

Ethers of cis or trans D-4-hydroxyproline (Hype), adjacent to octahydroindole-carboxylic acid (Oic), introduce a beta-turn into the backbone of peptides when positioned respectively at the i+1 and i+2 position of the turn. This is confirmed by NMR experiments performed on a model tetrapeptide in water. Synthetic alteration of the ether group allows simple probing of the steric limits and electrostatic potential of a receptor binding site, a technique applied successfully to the bradykinin receptor.